Antho-RFamide
Antho-RFamide结构式
|
常用名 | Antho-RFamide | 英文名 | Antho-RFamide |
|---|---|---|---|---|
| CAS号 | 107535-01-3 | 分子量 | 488.54000 | |
| 密度 | 1.48 g/cm3 | 沸点 | N/A | |
| 分子式 | C22H32N8O5 | 熔点 | N/A | |
| MSDS | 中文版 | 闪点 | N/A |
|
Isolation of pyroGlu-Gly-Arg-Phe-NH2 (Antho-RFamide), a neuropeptide from sea anemones.
Proc. Natl. Acad. Sci. U. S. A. 83 , 9817, (1986) A radioimmunoassay has been developed for peptides containing the carboxyl-terminal sequence Arg-Phe-NH2 (RFamide). Using this radioimmunoassay and applying cation-exchange chromatography and HPLC, we have isolated an RFamide peptide from acetic acid extracts... |
|
|
Excitatory action of the native neuropeptide antho-rfamide on muscles in the pennatulid Renilla köllikeri.
Gen. Pharmacol. 20(3) , 381-4, (1989) 1. Antho-RFamide (pGlu-Gly-Arg-Phe-amide), a neuropeptide recently isolated from the sea pansy Renilla köllikeri induced sustained (tonic) contractions in the rachis and peduncle of the colony, and in the individual autozooid polyps. 2. The threshold concentr... |
|
|
Antho-RFamide-containing neurons in the primitive nervous system of the anthozoan Renilla koellikeri.
J. Comp. Neurol. 472(2) , 208-20, (2004) The neuropeptide Antho-RFamide is extremely abundant in Renilla koellikeri (sea pansy), a representative of the cnidarians (octocorallians) considered to be closest to the stem ancestors of metazoans with nervous systems. Therefore, a knowledge of the distrib... |
|
|
Primary structure of the precursor for the anthozoan neuropeptide antho-RFamide from Renilla köllikeri: evidence for unusual processing enzymes.
J. Neurochem. 62(3) , 1214-22, (1994) Neuropeptides containing the C-terminal sequence Arg-Phe-NH2 are an important group of hormones mediating or modulating neuronal communication. Arg-Phe-NH2 peptides are abundant in evolutionarily "old" nervous systems such as those of coelenterates, the lowes... |
|
|
Monoamine release by neurons of a primitive nervous system: an amperometric study.
J. Neurochem. 76(6) , 1774-84, (2001) We measured monoamine release from dissociated neurons of the sea pansy Renilla koellikeri, a representative of the most evolutionarily ancient animals with nervous systems, by real-time monitoring of exocytosis using the amperometric method with carbon-fiber... |
|
|
Spawning and gamete follicle rupture in the cnidarian Renilla koellikeri: effects of putative neurohormones.
Gen. Comp. Endocrinol. 137(1) , 9-18, (2004) The neuroendocrine control of spawning (release of intact gamete follicles) and of the ensuing exfoliation (freeing of gametes by follicle epithelium rupture) was investigated in colonies of the sea pansy Renilla koellikeri, an octocorallian of the sea pen fa... |
|
|
Effects of three anthozoan neuropeptides, Antho-RWamide I, Antho-RWamide II and Antho-RFamide, on slow muscles from sea anemones.
J. Exp. Biol. 156 , 419-31, (1991) Antho-RWamide I (less than Glu-Ser-Leu-Arg-Trp-NH2) and Antho-RWamide II (less than Glu-Gly-Leu-Arg-Trp-NH2), the second and third anthozoan neuropeptides to be identified, both induced slow contractions of several endodermal muscles in four species of sea an... |
|
|
Identification of a novel type of processing sites in the precursor for the sea anemone neuropeptide Antho-RFamide ( J. Biol. Chem. 267(31) , 22534-41, (1992) Neuropeptides are synthesized as large precursor proteins that undergo posttranslational cleavages and modifications to produce bioactive peptides. Here, we have cloned two closely related precursor proteins for the sea anemone neuropeptide Antho-RFamide ( |
|
|
Primary structure of the precursor for the sea anemone neuropeptide Antho-RFamide (less than Glu-Gly-Arg-Phe-NH2).
Proc. Natl. Acad. Sci. U. S. A. 88(6) , 2555-9, (1991) Neuropeptides containing the carboxylterminal sequence Arg-Phe-NH2 are found throughout the animal kingdom and are important substances mediating neuronal communication. Here, we have cloned the cDNA coding for the precursor protein of the sea anemone neurope... |
|
|
Isolation of Antho-RFamide related peptides from the eyestalks of blue crab.
Comp. Biochem. Physiol.,. B. 104(2) , 235-40, (1993) 1. Two carboxyl-terminally amidated peptides (CP1 and CP2) were isolated from the blue crab (Callinectes sapidus) eyestalks by a method of carboxyl-terminal analysis. 2. The peptides were sequenced as pGlu-Gly-Arg-Phe-amide (CP1) and pGlu-Leu-Gly-Arg-Phe-amid... |